“Metallothionein-like” metal complexes in angiosperms; their structure and function
Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant p...
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| Autor*in: |
Robinson, N. J. [verfasserIn] Jackson, P. J. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1986 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Physiologia plantarum - Oxford [u.a.] : Wiley-Blackwell, 1948, 67(1986), 3, Seite 0 |
| Übergeordnetes Werk: |
volume:67 ; year:1986 ; number:3 ; pages:0 |
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| DOI / URN: |
10.1111/j.1399-3054.1986.tb05770.x |
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| 520 | |a Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant peptides, poly (γ-glutamylcysteinyl) glycines, (γEC)nG, have been discovered. These peptides bind metal ions, and in the presence of such ions the amount of (γEC), G in plant cells increases. The presence of peptide bonds through the γ-carboxyl group of glutamate, rather than the α-carboxyl group, suggests that these peptides are not encoded by structural genes but are the products of biosynthetic pathways. Cells which are resistant to supra-optimal concentrations of certain metal ions over-produce (γEC)n G. (γEC)n G. may be functional analogues of MT. Whether or not some plants also produce MT is an important question which remains to be answered. | ||
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10.1111/j.1399-3054.1986.tb05770.x doi (DE-627)NLEJ240969367 DE-627 ger DE-627 rakwb Robinson, N. J. verfasserin aut “Metallothionein-like” metal complexes in angiosperms; their structure and function Oxford, UK Blackwell Publishing Ltd 1986 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant peptides, poly (γ-glutamylcysteinyl) glycines, (γEC)nG, have been discovered. These peptides bind metal ions, and in the presence of such ions the amount of (γEC), G in plant cells increases. The presence of peptide bonds through the γ-carboxyl group of glutamate, rather than the α-carboxyl group, suggests that these peptides are not encoded by structural genes but are the products of biosynthetic pathways. Cells which are resistant to supra-optimal concentrations of certain metal ions over-produce (γEC)n G. (γEC)n G. may be functional analogues of MT. Whether or not some plants also produce MT is an important question which remains to be answered. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Angiosperms Jackson, P. J. verfasserin aut In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 67(1986), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:67 year:1986 number:3 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1986.tb05770.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 67 1986 3 0 |
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10.1111/j.1399-3054.1986.tb05770.x doi (DE-627)NLEJ240969367 DE-627 ger DE-627 rakwb Robinson, N. J. verfasserin aut “Metallothionein-like” metal complexes in angiosperms; their structure and function Oxford, UK Blackwell Publishing Ltd 1986 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant peptides, poly (γ-glutamylcysteinyl) glycines, (γEC)nG, have been discovered. These peptides bind metal ions, and in the presence of such ions the amount of (γEC), G in plant cells increases. The presence of peptide bonds through the γ-carboxyl group of glutamate, rather than the α-carboxyl group, suggests that these peptides are not encoded by structural genes but are the products of biosynthetic pathways. Cells which are resistant to supra-optimal concentrations of certain metal ions over-produce (γEC)n G. (γEC)n G. may be functional analogues of MT. Whether or not some plants also produce MT is an important question which remains to be answered. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Angiosperms Jackson, P. J. verfasserin aut In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 67(1986), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:67 year:1986 number:3 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1986.tb05770.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 67 1986 3 0 |
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10.1111/j.1399-3054.1986.tb05770.x doi (DE-627)NLEJ240969367 DE-627 ger DE-627 rakwb Robinson, N. J. verfasserin aut “Metallothionein-like” metal complexes in angiosperms; their structure and function Oxford, UK Blackwell Publishing Ltd 1986 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant peptides, poly (γ-glutamylcysteinyl) glycines, (γEC)nG, have been discovered. These peptides bind metal ions, and in the presence of such ions the amount of (γEC), G in plant cells increases. The presence of peptide bonds through the γ-carboxyl group of glutamate, rather than the α-carboxyl group, suggests that these peptides are not encoded by structural genes but are the products of biosynthetic pathways. Cells which are resistant to supra-optimal concentrations of certain metal ions over-produce (γEC)n G. (γEC)n G. may be functional analogues of MT. Whether or not some plants also produce MT is an important question which remains to be answered. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Angiosperms Jackson, P. J. verfasserin aut In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 67(1986), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:67 year:1986 number:3 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1986.tb05770.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 67 1986 3 0 |
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10.1111/j.1399-3054.1986.tb05770.x doi (DE-627)NLEJ240969367 DE-627 ger DE-627 rakwb Robinson, N. J. verfasserin aut “Metallothionein-like” metal complexes in angiosperms; their structure and function Oxford, UK Blackwell Publishing Ltd 1986 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant peptides, poly (γ-glutamylcysteinyl) glycines, (γEC)nG, have been discovered. These peptides bind metal ions, and in the presence of such ions the amount of (γEC), G in plant cells increases. The presence of peptide bonds through the γ-carboxyl group of glutamate, rather than the α-carboxyl group, suggests that these peptides are not encoded by structural genes but are the products of biosynthetic pathways. Cells which are resistant to supra-optimal concentrations of certain metal ions over-produce (γEC)n G. (γEC)n G. may be functional analogues of MT. Whether or not some plants also produce MT is an important question which remains to be answered. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Angiosperms Jackson, P. J. verfasserin aut In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 67(1986), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:67 year:1986 number:3 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1986.tb05770.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 67 1986 3 0 |
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10.1111/j.1399-3054.1986.tb05770.x doi (DE-627)NLEJ240969367 DE-627 ger DE-627 rakwb Robinson, N. J. verfasserin aut “Metallothionein-like” metal complexes in angiosperms; their structure and function Oxford, UK Blackwell Publishing Ltd 1986 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant peptides, poly (γ-glutamylcysteinyl) glycines, (γEC)nG, have been discovered. These peptides bind metal ions, and in the presence of such ions the amount of (γEC), G in plant cells increases. The presence of peptide bonds through the γ-carboxyl group of glutamate, rather than the α-carboxyl group, suggests that these peptides are not encoded by structural genes but are the products of biosynthetic pathways. Cells which are resistant to supra-optimal concentrations of certain metal ions over-produce (γEC)n G. (γEC)n G. may be functional analogues of MT. Whether or not some plants also produce MT is an important question which remains to be answered. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Angiosperms Jackson, P. J. verfasserin aut In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 67(1986), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:67 year:1986 number:3 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1986.tb05770.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 67 1986 3 0 |
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“Metallothionein-like” metal complexes in angiosperms; their structure and function |
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Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant peptides, poly (γ-glutamylcysteinyl) glycines, (γEC)nG, have been discovered. These peptides bind metal ions, and in the presence of such ions the amount of (γEC), G in plant cells increases. The presence of peptide bonds through the γ-carboxyl group of glutamate, rather than the α-carboxyl group, suggests that these peptides are not encoded by structural genes but are the products of biosynthetic pathways. Cells which are resistant to supra-optimal concentrations of certain metal ions over-produce (γEC)n G. (γEC)n G. may be functional analogues of MT. Whether or not some plants also produce MT is an important question which remains to be answered. |
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Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant peptides, poly (γ-glutamylcysteinyl) glycines, (γEC)nG, have been discovered. These peptides bind metal ions, and in the presence of such ions the amount of (γEC), G in plant cells increases. The presence of peptide bonds through the γ-carboxyl group of glutamate, rather than the α-carboxyl group, suggests that these peptides are not encoded by structural genes but are the products of biosynthetic pathways. Cells which are resistant to supra-optimal concentrations of certain metal ions over-produce (γEC)n G. (γEC)n G. may be functional analogues of MT. Whether or not some plants also produce MT is an important question which remains to be answered. |
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Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant peptides, poly (γ-glutamylcysteinyl) glycines, (γEC)nG, have been discovered. These peptides bind metal ions, and in the presence of such ions the amount of (γEC), G in plant cells increases. The presence of peptide bonds through the γ-carboxyl group of glutamate, rather than the α-carboxyl group, suggests that these peptides are not encoded by structural genes but are the products of biosynthetic pathways. Cells which are resistant to supra-optimal concentrations of certain metal ions over-produce (γEC)n G. (γEC)n G. may be functional analogues of MT. Whether or not some plants also produce MT is an important question which remains to be answered. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ240969367</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707123355.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1986 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1399-3054.1986.tb05770.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240969367</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Robinson, N. J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">“Metallothionein-like” metal complexes in angiosperms; their structure and function</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1986</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Evidence for the presence of the metal-binding protein metallothionein, MT, in higher plants is equivocal. Although a number of MT-like metal complexes have been isolated from plants, the chemical structures of most of these compounds have not been fully elucidated. Recently a novel class of plant peptides, poly (γ-glutamylcysteinyl) glycines, (γEC)nG, have been discovered. These peptides bind metal ions, and in the presence of such ions the amount of (γEC), G in plant cells increases. The presence of peptide bonds through the γ-carboxyl group of glutamate, rather than the α-carboxyl group, suggests that these peptides are not encoded by structural genes but are the products of biosynthetic pathways. Cells which are resistant to supra-optimal concentrations of certain metal ions over-produce (γEC)n G. (γEC)n G. may be functional analogues of MT. Whether or not some plants also produce MT is an important question which remains to be answered.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Angiosperms</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jackson, P. J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Physiologia plantarum</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1948</subfield><subfield code="g">67(1986), 3, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927738</subfield><subfield code="w">(DE-600)2020837-6</subfield><subfield code="x">1399-3054</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:67</subfield><subfield code="g">year:1986</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1399-3054.1986.tb05770.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">67</subfield><subfield code="j">1986</subfield><subfield code="e">3</subfield><subfield code="h">0</subfield></datafield></record></collection>
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